ID ADDA_BACSU Reviewed; 1232 AA.
AC P23478;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000303|PubMed:10756102};
DE EC=3.1.-.- {ECO:0000269|PubMed:10756102, ECO:0000269|PubMed:17570399};
DE EC=5.6.2.4 {ECO:0000269|PubMed:21071401};
DE AltName: Full=ATP-dependent helicase/nuclease AddA;
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000305};
GN Name=addA {ECO:0000303|PubMed:1646786, ECO:0000303|PubMed:9579061};
GN OrderedLocusNames=BSU10630;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OG1;
RX PubMed=1646786; DOI=10.1128/jb.173.12.3644-3655.1991;
RA Kooistra J., Venema G.;
RT "Cloning, sequencing, and expression of Bacillus subtilis genes involved in
RT ATP-dependent nuclease synthesis.";
RL J. Bacteriol. 173:3644-3655(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 780.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1000-1232.
RC STRAIN=168;
RX PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT degrees) in Bacillus subtilis.";
RL Microbiology 143:3305-3308(1997).
RN [6]
RP SUBUNIT, AND FUNCTION IN E.COLI.
RX PubMed=8387145; DOI=10.1111/j.1365-2958.1993.tb01182.x;
RA Kooistra J., Haijema B.J., Venema G.;
RT "The Bacillus subtilis addAB genes are fully functional in Escherichia
RT coli.";
RL Mol. Microbiol. 7:915-923(1993).
RN [7]
RP FUNCTION OF COMPLEX AS AN EXONUCLEASE AND HELICASE, COFACTOR, AND
RP ATP-DEPENDENCE.
RX PubMed=10756102; DOI=10.1006/jmbi.2000.3556;
RA Chedin F., Ehrlich S.D., Kowalczykowski S.C.;
RT "The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate
RT Chi sequence in vitro.";
RL J. Mol. Biol. 298:7-20(2000).
RN [8]
RP RECRUITS RECA TO DNA DOUBLE-STRAND BREAKS.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=16061691; DOI=10.1083/jcb.200412090;
RA Kidane D., Graumann P.L.;
RT "Dynamic formation of RecA filaments at DNA double strand break repair
RT centers in live cells.";
RL J. Cell Biol. 170:357-366(2005).
RN [9]
RP CHARACTERIZATION.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=16385024; DOI=10.1128/jb.188.2.353-360.2006;
RA Sanchez H., Kidane D., Castillo Cozar M., Graumann P.L., Alonso J.C.;
RT "Recruitment of Bacillus subtilis RecN to DNA double-strand breaks in the
RT absence of DNA end processing.";
RL J. Bacteriol. 188:353-360(2006).
RN [10]
RP FUNCTION AS A 3' -> 5' NUCLEASE, AND MUTAGENESIS OF LYS-36 AND ASP-1172.
RX PubMed=17570399; DOI=10.1016/j.jmb.2007.05.053;
RA Yeeles J.T.P., Dillingham M.S.;
RT "A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-
RT nucleases.";
RL J. Mol. Biol. 371:66-78(2007).
RN [11]
RP SUBUNIT, AND DNA-BINDING.
RX PubMed=19129187; DOI=10.1074/jbc.m808526200;
RA Yeeles J.T.P., Cammack R., Dillingham M.S.;
RT "An iron-sulfur cluster is essential for the binding of broken DNA by
RT AddAB-type helicase-nucleases.";
RL J. Biol. Chem. 284:7746-7755(2009).
RN [12]
RP FUNCTION AS A 3'-5' HELICASE, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF LYS-36 AND ASP-1172,
RP AND DNA-BINDING.
RX PubMed=21071401; DOI=10.1093/nar/gkq1124;
RA Yeeles J.T., Gwynn E.J., Webb M.R., Dillingham M.S.;
RT "The AddAB helicase-nuclease catalyses rapid and processive DNA unwinding
RT using a single Superfamily 1A motor domain.";
RL Nucleic Acids Res. 39:2271-2285(2011).
RN [13] {ECO:0007744|PDB:3U44, ECO:0007744|PDB:3U4Q}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF ADDAB IN COMPLEX WITH DS-DNA, AND
RP SUBUNIT.
RX PubMed=22307084; DOI=10.1038/emboj.2012.9;
RA Saikrishnan K., Yeeles J.T., Gilhooly N.S., Krajewski W.W.,
RA Dillingham M.S., Wigley D.B.;
RT "Insights into Chi recognition from the structure of an AddAB-type
RT helicase-nuclease complex.";
RL EMBO J. 31:1568-1578(2012).
RN [14] {ECO:0007744|PDB:4CEH, ECO:0007744|PDB:4CEI, ECO:0007744|PDB:4CEJ}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH DNA SUBSTRATES AND
RP ATP ANALOG, FUNCTION, PROBABLE REACTION MECHANISM, AND SUBUNIT.
RX PubMed=24670664; DOI=10.1038/nature13037;
RA Krajewski W.W., Fu X., Wilkinson M., Cronin N.B., Dillingham M.S.,
RA Wigley D.B.;
RT "Structural basis for translocation by AddAB helicase-nuclease and its
RT arrest at chi sites.";
RL Nature 508:416-419(2014).
CC -!- FUNCTION: An essential component of the DNA double-stranded break
CC repair machinery, the heterodimer acts both as a highly processive,
CC ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-
CC stranded exonuclease. Recognizes the B.subtilis Chi site (5'-AGCGG-3')
CC which transforms the enzyme from a helicase which degrades both DNA
CC strands to one with only 5' -> 3' exonuclease activity. This generates
CC a double-stranded DNA with a protruding 3'-terminated single-stranded
CC tail suitable for the initiation of homologous recombination (Chi
CC fragment). The AddA nuclease domain in particular is required for Chi
CC fragment generation; this subunit has 3' -> 5' nuclease and a helicase
CC motor with 3' -> 5' helicase activity (PubMed:17570399,
CC PubMed:21071401). The 3'-5' helicase activity of isolated AddA acts on
CC 3'-tailed substrate and requires AddB to bind to blunt-ended DNA
CC (PubMed:21071401). RecA thread formation during DNA double-strand break
CC repair requires RecJ or AddAB (PubMed:16385024).
CC {ECO:0000269|PubMed:10756102, ECO:0000269|PubMed:16385024,
CC ECO:0000269|PubMed:17570399, ECO:0000269|PubMed:21071401,
CC ECO:0000269|PubMed:24670664, ECO:0000269|PubMed:8387145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000269|PubMed:21071401};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000269|PubMed:21071401};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10756102};
CC Note=At low magnesium concentrations there is no nuclease activity, but
CC helicase activity is unaffected (PubMed:10756102, PubMed:19129187,
CC PubMed:21071401). {ECO:0000269|PubMed:10756102,
CC ECO:0000269|PubMed:21071401};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.16 uM for ATP {ECO:0000269|PubMed:21071401};
CC Note=kcat for ATP hydrolysis by AddAB is 88 sec(-1), ATPase is
CC strongly stimulated by ssDNA. {ECO:0000269|PubMed:21071401};
CC -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000269|PubMed:19129187,
CC ECO:0000269|PubMed:21071401, ECO:0000269|PubMed:22307084,
CC ECO:0000269|PubMed:24670664, ECO:0000269|PubMed:8387145}.
CC -!- INTERACTION:
CC P23478; P23477: addB; NbExp=4; IntAct=EBI-16098568, EBI-5247995;
CC -!- MISCELLANEOUS: This enzyme is a functional homolog of the E.coli RecBCD
CC enzyme; unlike the RecBCD enzyme it degrades both duplex strands
CC symmetrically.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000305}.
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DR EMBL; M63489; AAA22201.1; -; Genomic_DNA.
DR EMBL; Y14081; CAA74482.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12903.2; -; Genomic_DNA.
DR EMBL; Y09476; CAA70668.1; -; Genomic_DNA.
DR PIR; B39432; B39432.
DR RefSeq; NP_388944.2; NC_000964.3.
DR RefSeq; WP_003233100.1; NZ_JNCM01000035.1.
DR PDB; 3U44; X-ray; 3.20 A; A=1-1232.
DR PDB; 3U4Q; X-ray; 2.80 A; A=1-1232.
DR PDB; 4CEH; X-ray; 3.24 A; A=1-1232.
DR PDB; 4CEI; X-ray; 2.80 A; A=1-1232.
DR PDB; 4CEJ; X-ray; 3.00 A; A=1-1232.
DR PDBsum; 3U44; -.
DR PDBsum; 3U4Q; -.
DR PDBsum; 4CEH; -.
DR PDBsum; 4CEI; -.
DR PDBsum; 4CEJ; -.
DR AlphaFoldDB; P23478; -.
DR SMR; P23478; -.
DR DIP; DIP-60825N; -.
DR IntAct; P23478; 1.
DR STRING; 224308.BSU10630; -.
DR PaxDb; 224308-BSU10630; -.
DR EnsemblBacteria; CAB12903; CAB12903; BSU_10630.
DR GeneID; 939793; -.
DR KEGG; bsu:BSU10630; -.
DR PATRIC; fig|224308.179.peg.1143; -.
DR eggNOG; COG1074; Bacteria.
DR InParanoid; P23478; -.
DR OrthoDB; 9810135at2; -.
DR PhylomeDB; P23478; -.
DR BioCyc; BSUB:BSU10630-MONOMER; -.
DR BRENDA; 3.6.4.12; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; AddA.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA repair; DNA-binding;
KW Exonuclease; Helicase; Hydrolase; Isomerase; Nuclease; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1232
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000064449"
FT DOMAIN 9..481
FT /note="UvrD-like helicase ATP-binding"
FT DOMAIN 508..798
FT /note="UvrD-like helicase C-terminal"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24670664,
FT ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24670664,
FT ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24670664,
FT ECO:0000312|PDB:4CEI"
FT BINDING 478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24670664,
FT ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ"
FT BINDING 479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24670664,
FT ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ"
FT BINDING 541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ"
FT BINDING 573
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ"
FT BINDING 873
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24670664,
FT ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ"
FT MUTAGEN 36
FT /note="K->A: Loss of helicase and nuclease activity. DNA-
FT binding is unaltered. Dramatically decreases ATPase
FT activity, kcat for ATP hydrolysis is 4.64 min(-1), loss of
FT helicase activity."
FT /evidence="ECO:0000269|PubMed:17570399,
FT ECO:0000269|PubMed:21071401"
FT MUTAGEN 1172
FT /note="D->A: Loss of 3'-5' nuclease activity, helicase and
FT DNA-binding are unaltered. No production of Chi fragments;
FT when associated with A-961 in AddB nearly complete loss of
FT both nuclease activities."
FT /evidence="ECO:0000269|PubMed:17570399,
FT ECO:0000269|PubMed:21071401"
FT CONFLICT 780
FT /note="A -> G (in Ref. 1; AAA22201 and 2; CAA74482)"
FT /evidence="ECO:0000305"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 67..87
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 135..156
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 219..243
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 256..269
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 307..323
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 328..362
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:4CEI"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 392..400
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 414..423
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:4CEI"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 445..448
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:4CEI"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 482..493
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 524..530
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 546..563
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 568..571
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:4CEI"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:4CEI"
FT STRAND 585..594
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 595..604
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:4CEJ"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 621..634
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 639..647
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 655..662
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 670..680
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 686..707
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 710..721
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 723..727
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 733..750
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 752..754
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 758..770
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 783..786
FT /evidence="ECO:0007829|PDB:4CEI"
FT STRAND 788..792
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 796..798
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 801..807
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 816..819
FT /evidence="ECO:0007829|PDB:4CEI"
FT STRAND 820..825
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 826..828
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 829..832
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 834..836
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 837..840
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 841..843
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 846..872
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 874..883
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 887..897
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 901..904
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 907..911
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 917..925
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 926..928
FT /evidence="ECO:0007829|PDB:4CEH"
FT HELIX 940..944
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 949..954
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 956..959
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 973..978
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 991..999
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1005..1007
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1010..1016
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 1048..1050
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1057..1068
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1079..1091
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1097..1102
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1105..1109
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1110..1113
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1115..1121
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1124..1137
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1138..1140
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1147..1149
FT /evidence="ECO:0007829|PDB:4CEI"
FT STRAND 1151..1163
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1168..1174
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 1183..1185
FT /evidence="ECO:0007829|PDB:4CEJ"
FT TURN 1187..1189
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1190..1196
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1198..1212
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1216..1223
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 1224..1227
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1228..1231
FT /evidence="ECO:0007829|PDB:3U4Q"
SQ SEQUENCE 1232 AA; 141087 MW; 2A1B70FA4E645FE4 CRC64;
MNIPKPADST WTDDQWNAIV STGQDILVAA AAGSGKTAVL VERMIRKITA EENPIDVDRL
LVVTFTNASA AEMKHRIAEA LEKELVQRPG SLHIRRQLSL LNRASISTLH SFCLQVLKKY
YYLIDLDPGF RIADQTEGEL IGDEVLDELF EDEYAKGEKA FFELVDRYTT DRHDLDLQFL
VKQVYEYSRS HPNPEAWLES FVHLYDVSEK SAIEELPFYQ YVKEDIAMVL NGAKEKLLRA
LELTKAPGGP APRADNFLDD LAQIDELIQH QDDFSELYKR VPAVSFKRAK AVKGDEFDPA
LLDEATDLRN GAKKLLEKLK TDYFTRSPEQ HLKSLAEMKP VIETLVQLVI SYGKRFEAAK
QEKSIIDFSD LEHYCLAILT AENDKGEREP SEAARFYQEQ FHEVLVDEYQ DTNLVQESIL
QLVTSGPEET GNLFMVGDVK QSIYRFRLAE PLLFLSKYKR FTESGEGTGR KIDLNKNFRS
RADILDSTNF LFKQLMGGKI GEVDYDEQAE LKLGAAYPDN DETETELLLI DNAEDTDASE
EAEELETVQF EAKAIAKEIR KLISSPFKVY DGKKKTHRNI QYRDIVILLR SMPWAPQIME
ELRAQGIPVY ANLTSGYFEA VEVAVALSVL KVIDNPYQDI PLASVLRSPI VGADENELSL
IRLENKKAPY YEAMKDYLAA GDRSDELYQK LNTFYGHLQK WRAFSKNHSV SELIWEVYRD
TKYMDYVGGM PGGKQRQANL RVLYDRARQY ESTAFRGLFR FLRFIERMQE RGDDLGTARA
LSEQEDVVRL MTIHSSKGLE FPVVFVAGLG RNFNMMDLNK SYLLDKELGF GTKYIHPQLR
ISYPTLPLIA MKKKMRRELL SEELRVLYVA LTRAKEKLFL IGSCKDHQKQ LAKWQASASQ
TDWLLPEFDR YQARTYLDFI GPALARHRDL GDLAGVPAHA DISGHPARFA VQMIHSYDLL
DDDLEERMEE KSERLEAIRR GEPVPGSFAF DEKAREQLSW TYPHQEVTQI RTKQSVSEIK
RKREYEDEYS GRAPVKPADG SILYRRPAFM MKKGLTAAEK GTAMHTVMQH IPLSHVPSIE
EAEQTVHRLY EKELLTEEQK DAIDIEEIVQ FFHTEIGGQL IGAKWKDREI PFSLALPAKE
IYPDAHEADE PLLVQGIIDC LYETEDGLYL LDYKSDRIEG KFQHGFEGAA PILKKRYETQ
IQLYTKAVEQ IAKTKVKGCA LYFFDGGHIL TL
//
